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8.A.14.1.4
Auxillary β subunit (β3) of voltage-dependent and Ca2+ sensitive K+ channel (MaxiK; 1.A.1.3.2) (Brenner et al., 2000).  44% identical to TC# 8.A.14.1.3.

Accession Number:Q9NPA1
Protein Name:Calcium-activated potassium channel subunit beta 3 aka β3
Length:279
Molecular Weight:31604.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:2
Location1 / Topology2 / Orientation3: Membrane1 / Multi-pass membrane protein2
Substrate NONE

Cross database links:

Genevestigator: Q9NPA1
eggNOG: prNOG08712
HEGENOM: HBG446091
RefSeq: NP_055222.3    NP_741979.1    NP_741980.1    NP_741981.1   
Entrez Gene ID: 27094   
Pfam: PF03185   
Drugbank: Drugbank Link   
OMIM: 605222  gene

Gene Ontology

GO:0008076 C:voltage-gated potassium channel complex
GO:0015269 F:calcium-activated potassium channel activity
GO:0015459 F:potassium channel regulator activity
GO:0005513 P:detection of calcium ion
GO:0006813 P:potassium ion transport
GO:0019228 P:regulation of action potential in neuron

References (11)

[1] “Identification of a putative regulatory subunit of a calcium-activated potassium channel in the dup(3q) syndrome region and a related sequence on 22q11.2.”  Riazi M.A.et.al.   10585773
[2] “Cloning and functional characterization of novel large conductance calcium-activated potassium channel beta subunits, hKCNMB3 and hKCNMB4.”  Brenner R.et.al.   10692449
[3] “Cloning and functional expression of two families of Beta-subunits of the large conductance calcium-activated potassium channel.”  Uebele V.N.et.al.   10766764
[4] “A neuronal beta subunit (KCNMB4) makes the large conductance, voltage- and Ca2+-activated K+ channel resistant to charybdotoxin and iberiotoxin.”  Meera P.et.al.   10792058
[5] “hKCNMB3 and hKCNMB4, cloning and characterization of two members of the large-conductance calcium-activated potassium channel beta subunit family.”  Behrens R.et.al.   10828459
[6] “Rectification and rapid activation at low Ca2+ of Ca2+-activated, voltage-dependent BK currents: consequences of rapid inactivation by a novel beta subunit.”  Xia X.-M.et.al.   10864947
[7] “Inactivation of BK channels mediated by the NH(2) terminus of the beta3b auxiliary subunit involves a two-step mechanism: possible separation of binding and blockade.”  Lingle C.J.et.al.   11382808
[8] “Gating properties conferred on BK channels by the beta3b auxiliary subunit in the absence of its NH(2)- and COOH termini.”  Zeng X.-H.et.al.   11382809
[9] “Variants of the KCNMB3 regulatory subunit of maxi BK channels affect channel inactivation.”  Hu S.et.al.   14612589
[10] “Redox-sensitive extracellular gates formed by auxiliary beta subunits of calcium-activated potassium channels.”  Zeng X.-H.et.al.   12740608
[11] “New disguises for an old channel: MaxiK channel beta-subunits.”  Orio P.et.al.   12136044

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MDFSPSSELG FHFVAFILLT RHRTAFPASG KKRETDYSDG DPLDVHKRLP SSAGEDRAVM 
61:	LGFAMMGFSV LMFFLLGTTI LKPFMLSIQR EESTCTAIHT DIMDDWLDCA FTCGVHCHGQ 
121:	GKYPCLQVFV NLSHPGQKAL LHYNEEAVQI NPKCFYTPKC HQDRNDLLNS ALDIKEFFDH 
181:	KNGTPFSCFY SPASQSEDVI LIKKYDQMAI FHCLFWPSLT LLGGALIVGM VRLTQHLSLL 
241:	CEKYSTVVRD EVGGKVPYIE QHQFKLCIMR RSKGRAEKS